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Q2M3T9

- HYAL4_HUMAN

UniProt

Q2M3T9 - HYAL4_HUMAN

Protein

Hyaluronidase-4

Gene

HYAL4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 2 (11 Sep 2007)
      Previous versions | rss
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    Functioni

    Endo-hyaluronidase that degrades hyaluronan to smaller oligosaccharide fragments. Has also chondroitin sulfate hydrolase activity, The best substrate being the galactosaminidic linkage in the sequence of a trisulfated tetrasaccharide.2 Publications

    Catalytic activityi

    Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.

    pH dependencei

    Optimum pH is 4.5-5 (for chondroitin sulfate hydrolase activity).1 Publication

    Temperature dependencei

    Optimum temperature is 37 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei147 – 1471Proton donorBy similarity

    GO - Molecular functioni

    1. hyalurononglucosaminidase activity Source: ProtInc

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. chondroitin sulfate catabolic process Source: Ensembl
    3. glycosaminoglycan catabolic process Source: ProtInc

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02883-MONOMER.

    Protein family/group databases

    CAZyiGH56. Glycoside Hydrolase Family 56.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hyaluronidase-4 (EC:3.2.1.35)
    Short name:
    Hyal-4
    Alternative name(s):
    Chondroitin sulfate endo-beta-N-acetylgalactosaminidase
    Chondroitin sulfate hydrolase
    Short name:
    CSHY
    Hyaluronoglucosaminidase-4
    Gene namesi
    Name:HYAL4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:5323. HYAL4.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29574.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 481481Hyaluronidase-4PRO_0000301999Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi59 ↔ 351By similarity
    Glycosylationi86 – 861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi177 – 1771N-linked (GlcNAc...) (complex)1 Publication
    Disulfide bondi223 ↔ 237By similarity
    Glycosylationi343 – 3431N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi376 ↔ 387By similarity
    Disulfide bondi381 ↔ 435By similarity
    Disulfide bondi437 ↔ 446By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ2M3T9.
    PRIDEiQ2M3T9.

    PTM databases

    PhosphoSiteiQ2M3T9.

    Expressioni

    Tissue specificityi

    Detected in placenta and skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiQ2M3T9.
    BgeeiQ2M3T9.
    CleanExiHS_HYAL4.
    GenevestigatoriQ2M3T9.

    Organism-specific databases

    HPAiHPA029453.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000223026.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2M3T9.
    SMRiQ2M3T9. Positions 48-363.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 88CytoplasmicSequence Analysis
    Topological domaini30 – 453424ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini475 – 4817CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei9 – 2921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei454 – 47421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 56 family.Curated

    Keywords - Domaini

    EGF-like domain, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG77606.
    HOGENOMiHOG000015133.
    HOVERGENiHBG052053.
    InParanoidiQ2M3T9.
    KOiK01197.
    OMAiWNTKDVY.
    PhylomeDBiQ2M3T9.
    TreeFamiTF321598.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR000742. EG-like_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR018155. Hyaluronidase.
    [Graphical view]
    PANTHERiPTHR11769. PTHR11769. 1 hit.
    PfamiPF01630. Glyco_hydro_56. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038193. Hyaluronidase. 1 hit.
    PRINTSiPR00846. GLHYDRLASE56.
    SMARTiSM00181. EGF. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q2M3T9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVLSEGQLK LCVVQPVHLT SWLLIFFILK SISCLKPARL PIYQRKPFIA    50
    AWNAPTDQCL IKYNLRLNLK MFPVIGSPLA KARGQNVTIF YVNRLGYYPW 100
    YTSQGVPING GLPQNISLQV HLEKADQDIN YYIPAEDFSG LAVIDWEYWR 150
    PQWARNWNSK DVYRQKSRKL ISDMGKNVSA TDIEYLAKVT FEESAKAFMK 200
    ETIKLGIKSR PKGLWGYYLY PDCHNYNVYA PNYSGSCPED EVLRNNELSW 250
    LWNSSAALYP SIGVWKSLGD SENILRFSKF RVHESMRIST MTSHDYALPV 300
    FVYTRLGYRD EPLFFLSKQD LVSTIGESAA LGAAGIVIWG DMNLTASKAN 350
    CTKVKQFVSS DLGSYIANVT RAAEVCSLHL CRNNGRCIRK MWNAPSYLHL 400
    NPASYHIEAS EDGEFTVKGK ASDTDLAVMA DTFSCHCYQG YEGADCREIK 450
    TADGCSGVSP SPGSLMTLCL LLLASYRSIQ L 481
    Length:481
    Mass (Da):54,249
    Last modified:September 11, 2007 - v2
    Checksum:i9D530009AA898D1F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti263 – 2631G → C in AAC98883. (PubMed:10493834)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti346 – 3461A → S.1 Publication
    Corresponds to variant rs6949082 [ dbSNP | Ensembl ].
    VAR_034936

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF009010 mRNA. Translation: AAC98883.1.
    AB470346 mRNA. Translation: BAI49593.1.
    AC006029 Genomic DNA. Translation: AAD43186.1.
    CH236947 Genomic DNA. Translation: EAL24331.1.
    CH471070 Genomic DNA. Translation: EAW83603.1.
    BC104788 mRNA. Translation: AAI04789.1.
    BC104790 mRNA. Translation: AAI04791.1.
    CCDSiCCDS5789.1.
    RefSeqiNP_036401.2. NM_012269.2.
    XP_005250295.1. XM_005250238.1.
    UniGeneiHs.28673.

    Genome annotation databases

    EnsembliENST00000223026; ENSP00000223026; ENSG00000106302.
    ENST00000476325; ENSP00000417186; ENSG00000106302.
    GeneIDi23553.
    KEGGihsa:23553.
    UCSCiuc003vlc.3. human.

    Polymorphism databases

    DMDMi158564281.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF009010 mRNA. Translation: AAC98883.1 .
    AB470346 mRNA. Translation: BAI49593.1 .
    AC006029 Genomic DNA. Translation: AAD43186.1 .
    CH236947 Genomic DNA. Translation: EAL24331.1 .
    CH471070 Genomic DNA. Translation: EAW83603.1 .
    BC104788 mRNA. Translation: AAI04789.1 .
    BC104790 mRNA. Translation: AAI04791.1 .
    CCDSi CCDS5789.1.
    RefSeqi NP_036401.2. NM_012269.2.
    XP_005250295.1. XM_005250238.1.
    UniGenei Hs.28673.

    3D structure databases

    ProteinModelPortali Q2M3T9.
    SMRi Q2M3T9. Positions 48-363.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000223026.

    Protein family/group databases

    CAZyi GH56. Glycoside Hydrolase Family 56.

    PTM databases

    PhosphoSitei Q2M3T9.

    Polymorphism databases

    DMDMi 158564281.

    Proteomic databases

    PaxDbi Q2M3T9.
    PRIDEi Q2M3T9.

    Protocols and materials databases

    DNASUi 23553.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000223026 ; ENSP00000223026 ; ENSG00000106302 .
    ENST00000476325 ; ENSP00000417186 ; ENSG00000106302 .
    GeneIDi 23553.
    KEGGi hsa:23553.
    UCSCi uc003vlc.3. human.

    Organism-specific databases

    CTDi 23553.
    GeneCardsi GC07P123469.
    H-InvDB HIX0033519.
    HGNCi HGNC:5323. HYAL4.
    HPAi HPA029453.
    MIMi 604510. gene.
    neXtProti NX_Q2M3T9.
    PharmGKBi PA29574.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG77606.
    HOGENOMi HOG000015133.
    HOVERGENi HBG052053.
    InParanoidi Q2M3T9.
    KOi K01197.
    OMAi WNTKDVY.
    PhylomeDBi Q2M3T9.
    TreeFami TF321598.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS02883-MONOMER.

    Miscellaneous databases

    GenomeRNAii 23553.
    NextBioi 46112.
    PROi Q2M3T9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q2M3T9.
    Bgeei Q2M3T9.
    CleanExi HS_HYAL4.
    Genevestigatori Q2M3T9.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR000742. EG-like_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR018155. Hyaluronidase.
    [Graphical view ]
    PANTHERi PTHR11769. PTHR11769. 1 hit.
    Pfami PF01630. Glyco_hydro_56. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038193. Hyaluronidase. 1 hit.
    PRINTSi PR00846. GLHYDRLASE56.
    SMARTi SM00181. EGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression analysis of six paralogous human hyaluronidase genes clustered on chromosomes 3p21 and 7q31."
      Csoka A.B., Scherer S.W., Stern R.
      Genomics 60:356-361(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "Identification of human hyaluronidase-4 as a novel chondroitin sulfate hydrolase that preferentially cleaves the galactosaminidic linkage in the trisulfated tetrasaccharide sequence."
      Kaneiwa T., Mizumoto S., Sugahara K., Yamada S.
      Glycobiology 20:300-309(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    3. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-346.
      Tissue: Cerebellum.
    7. "Structures of vertebrate hyaluronidases and their unique enzymatic mechanism of hydrolysis."
      Jedrzejas M.J., Stern R.
      Proteins 61:227-238(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, 3D-STRUCTURE MODELING.
    8. Cited for: GLYCOSYLATION AT ASN-177.

    Entry informationi

    Entry nameiHYAL4_HUMAN
    AccessioniPrimary (citable) accession number: Q2M3T9
    Secondary accession number(s): D0VXG1, Q9UL99, Q9Y6T9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 80 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3